ID   CLP5_ARATH              Reviewed;         424 AA.
AC   Q9FLE2;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   10-OCT-2018, entry version 92.
DE   RecName: Full=Protein CLP1 homolog 5 {ECO:0000255|HAMAP-Rule:MF_03035};
DE   AltName: Full=CLP-like protein 5;
DE   AltName: Full=Protein CLP-SIMILAR PROTEIN 5;
GN   Name=CLPS5 {ECO:0000303|PubMed:18479511};
GN   OrderedLocusNames=At5g39930 {ECO:0000312|Araport:AT5G39930};
GN   ORFNames=MYH19.12 {ECO:0000312|EMBL:BAB10217.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV.
RT   Sequence features of the regions of 1,456,315 bp covered by nineteen
RT   physically assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Underwood B.A., Xiao Y., Moskal W., Monaghan E., Wang W., Redman J.,
RA   Wu H.C., Utterback T., Town C.D.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   INTERACTION WITH PCFS1; FIPS3 AND CPSF30, GENE FAMILY, AND
RP   NOMENCLATURE.
RX   PubMed=18479511; DOI=10.1186/1471-2164-9-220;
RA   Hunt A.G., Xu R., Addepalli B., Rao S., Forbes K.P., Meeks L.R.,
RA   Xing D., Mo M., Zhao H., Bandyopadhyay A., Dampanaboina L., Marion A.,
RA   Von Lanken C., Li Q.Q.;
RT   "Arabidopsis mRNA polyadenylation machinery: comprehensive analysis of
RT   protein-protein interactions and gene expression profiling.";
RL   BMC Genomics 9:220-220(2008).
CC   -!- FUNCTION: Required for endonucleolytic cleavage during
CC       polyadenylation-dependent pre-mRNA 3'-end formation.
CC       {ECO:0000255|HAMAP-Rule:MF_03035}.
CC   -!- SUBUNIT: Forms a complex with cleavage and polyadenylation
CC       specificity factor (CPSF) subunits PCFS1, FIPS3 and CPSF30.
CC       {ECO:0000269|PubMed:18479511}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9SR06,
CC       ECO:0000255|HAMAP-Rule:MF_03035}.
CC   -!- SIMILARITY: Belongs to the Clp1 family. Clp1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03035}.
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DR   EMBL; AB010077; BAB10217.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94492.1; -; Genomic_DNA.
DR   EMBL; AY954872; AAX55198.1; -; mRNA.
DR   RefSeq; NP_198809.2; NM_123356.3.
DR   UniGene; At.55267; -.
DR   ProteinModelPortal; Q9FLE2; -.
DR   SMR; Q9FLE2; -.
DR   BioGrid; 19241; 1.
DR   IntAct; Q9FLE2; 1.
DR   STRING; 3702.AT5G39930.1; -.
DR   PaxDb; Q9FLE2; -.
DR   EnsemblPlants; AT5G39930.1; AT5G39930.1; AT5G39930.
DR   GeneID; 833990; -.
DR   Gramene; AT5G39930.1; AT5G39930.1; AT5G39930.
DR   KEGG; ath:AT5G39930; -.
DR   Araport; AT5G39930; -.
DR   TAIR; locus:2178072; AT5G39930.
DR   eggNOG; KOG2749; Eukaryota.
DR   eggNOG; COG5623; LUCA.
DR   HOGENOM; HOG000231935; -.
DR   InParanoid; Q9FLE2; -.
DR   KO; K14399; -.
DR   OMA; VQTIDPT; -.
DR   OrthoDB; EOG0936095Q; -.
DR   PhylomeDB; Q9FLE2; -.
DR   Reactome; R-ATH-72163; mRNA Splicing - Major Pathway.
DR   PRO; PR:Q9FLE2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FLE2; baseline and differential.
DR   Genevisible; Q9FLE2; AT.
DR   GO; GO:0005849; C:mRNA cleavage factor complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; IBA:GO_Central.
DR   GO; GO:0006379; P:mRNA cleavage; IBA:GO_Central.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IBA:GO_Central.
DR   Gene3D; 2.60.120.1030; -; 1.
DR   Gene3D; 3.30.70.2410; -; 1.
DR   HAMAP; MF_03035; Clp1; 1.
DR   InterPro; IPR028606; Clp1.
DR   InterPro; IPR010655; Clp1_C.
DR   InterPro; IPR038238; Clp1_C_sf.
DR   InterPro; IPR032324; Clp1_N.
DR   InterPro; IPR038239; Clp1_N_sf.
DR   InterPro; IPR032319; CLP1_P.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF06807; Clp1; 1.
DR   Pfam; PF16573; CLP1_N; 1.
DR   Pfam; PF16575; CLP1_P; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; mRNA processing; Nucleotide-binding;
KW   Nucleus; Reference proteome.
FT   CHAIN         1    424       Protein CLP1 homolog 5.
FT                                /FTId=PRO_0000431352.
FT   NP_BIND     124    129       ATP. {ECO:0000255|HAMAP-Rule:MF_03035}.
FT   BINDING      16     16       ATP. {ECO:0000255|HAMAP-Rule:MF_03035}.
FT   BINDING      56     56       ATP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03035}.
SQ   SEQUENCE   424 AA;  47489 MW;  50CC9AE9B42B32C9 CRC64;
     MFGPQIRRVK LEKQSELRIE LQPTSPLRLR LLDGKAEIFG YELPHEVWIT FPPLMTFAVF
     TWYGATIEID GITGNEYISC ETPMVNYLGL HNSLQVQRHR VTSSTRDSAS SQEGPRVIIV
     GDIDSGKSTL AKMLLNWAVK DGWKPTFVDL NVGQSSITIP GTIAAAPIKM LVDPVEGFPL
     DKALIHYFGL TNPSVNLRLY RTLVEELARE LKEEFSANAE SRASGMVIDT MGFIVREGYA
     LLLHAIRTFN ASLVIVVGQE EKLVYDLKKN LKFKKNLQVL NLEKSEGVFS RSSDFRKTLR
     NSNIQNYFYG VTNDLTVYTK TVKFSDVQVY RIGDFRVSGS TSAHQRGNDP LKITLVTIDE
     HLVNKVLAIS YAIKPDQIIS SIVAGFVCIK NVDISEERIT YVSPSAAELP SKILILGTLT
     WHVT
//